Copper binding to the PrP isoforms: a putative marker of their conformation and function

Citation
Y. Shaked et al., Copper binding to the PrP isoforms: a putative marker of their conformation and function, J VIROLOGY, 75(17), 2001, pp. 7872-7874
Citations number
16
Categorie Soggetti
Microbiology
Journal title
JOURNAL OF VIROLOGY
ISSN journal
0022538X → ACNP
Volume
75
Issue
17
Year of publication
2001
Pages
7872 - 7874
Database
ISI
SICI code
0022-538X(200109)75:17<7872:CBTTPI>2.0.ZU;2-F
Abstract
We show here that PrPC, the normal isoform of the prion protein (PrPSc), co uld be retained by a Cu2+-loaded resin through two different binding sites. Contrarily, PrPSc was not retained at all by such resin. This constitutes a new prion-specific property of PrPSc, which in addition to protease resis tance and beta -sheet content, may result from its aberrant conformation.